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CheR methyltransferase, all-alpha domain
CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase. [1]. 9115443. Crystal structure of the chemotaxis receptor methyltransferase. CheR suggests a conserved structural motif for binding. S-adenosylmethionine.. Djordjevic S, Stock AM;. Structure 1997;5:545-558. (from Pfam)
CheR family methyltransferase
CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM. [1]. 9115443. Crystal structure of the chemotaxis receptor methyltransferase. CheR suggests a conserved structural motif for binding. S-adenosylmethionine.. Djordjevic S, Stock AM;. Structure 1997;5:545-558. (from Pfam)
CheR family methyltransferase is a class I SAM-dependent methyltransferase that catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; such as chemotaxis protein methyltransferase that methylates membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP
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